Nardilysin

Nardilysin (EC 3.4.24.61, N-arginine dibasic convertase, NRD-convertase) is an enzyme.[1][2][3][4] This enzyme catalyses the following chemical reaction

Hydrolysis of polypeptides, preferably at -Xaa-Arg-Lys-, and less commonly at -Arg-Arg-Xaa-, in which Xaa is not Arg or Lys
Nardilysin
Identifiers
EC number3.4.24.61
CAS number292850-69-2
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum

This enzyme is present rat brain and testis.

References
  1. Gomez S, Gluschankof P, Morel A, Cohen P (September 1985). "The somatostatin-28 convertase of rat brain cortex is associated with secretory granule membranes". The Journal of Biological Chemistry. 260 (19): 10541–5. PMID 3897221.
  2. Gluschankof P, Gomez S, Morel A, Cohen P (July 1987). "Enzymes that process somatostatin precursors. A novel endoprotease that cleaves before the arginine-lysine doublet is involved in somatostatin-28 convertase activity of rat brain cortex". The Journal of Biological Chemistry. 262 (20): 9615–20. PMID 2885328.
  3. Chesneau V, Pierotti AR, Barré N, Créminon C, Tougard C, Cohen P (January 1994). "Isolation and characterization of a dibasic selective metalloendopeptidase from rat testes that cleaves at the amino terminus of arginine residues". The Journal of Biological Chemistry. 269 (3): 2056–61. PMID 8294457.
  4. Pierotti AR, Prat A, Chesneau V, Gaudoux F, Leseney AM, Foulon T, Cohen P (June 1994). "N-arginine dibasic convertase, a metalloendopeptidase as a prototype of a class of processing enzymes". Proceedings of the National Academy of Sciences of the United States of America. 91 (13): 6078–82. doi:10.1073/pnas.91.13.6078. PMC 44141. PMID 8016118.
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